TY - JOUR
T1 - Structure of Lumazine Protein, an Optical Transponder of Luminescent Bacteria
AU - Chatwell, Lorenz
AU - Illarionova, Victoria
AU - Illarionov, Boris
AU - Eisenreich, Wolfgang
AU - Huber, Robert
AU - Skerra, Arne
AU - Bacher, Adelbert
AU - Fischer, Markus
N1 - Funding Information:
This work was supported by grants from the Deutsche Forschungsgemeinschaft (Project No. FI 824/2-1,2), the Fonds der Chemischen Industrie and the Hans-Fischer-Gesellschaft e.V.
PY - 2008/9/26
Y1 - 2008/9/26
N2 - The intensely fluorescent lumazine protein is believed to be involved in the bioluminescence of certain marine bacteria. The sequence of the catalytically inactive protein resembles that of the enzyme riboflavin synthase. Its non-covalently bound fluorophore, 6,7-dimethyl-8-ribityllumazine, is the substrate of this enzyme and also the committed precursor of vitamin B2. An extensive crystallization screen was performed using numerous single-site mutants of the lumazine protein from Photobacterium leiognathi in complex with its fluorophore and with riboflavin, respectively. Only the L49N mutant in complex with riboflavin yielded suitable crystals, allowing X-ray structure determination to a resolution of 2.5 Å. The monomeric protein folds into two closely similar domains that are structurally related by pseudo-C2 symmetry, whereby the entire domain topology resembles that of riboflavin synthase. Riboflavin is bound to a shallow cavity in the N-terminal domain of lumazine protein, whereas the C-terminal domain lacks a ligand.
AB - The intensely fluorescent lumazine protein is believed to be involved in the bioluminescence of certain marine bacteria. The sequence of the catalytically inactive protein resembles that of the enzyme riboflavin synthase. Its non-covalently bound fluorophore, 6,7-dimethyl-8-ribityllumazine, is the substrate of this enzyme and also the committed precursor of vitamin B2. An extensive crystallization screen was performed using numerous single-site mutants of the lumazine protein from Photobacterium leiognathi in complex with its fluorophore and with riboflavin, respectively. Only the L49N mutant in complex with riboflavin yielded suitable crystals, allowing X-ray structure determination to a resolution of 2.5 Å. The monomeric protein folds into two closely similar domains that are structurally related by pseudo-C2 symmetry, whereby the entire domain topology resembles that of riboflavin synthase. Riboflavin is bound to a shallow cavity in the N-terminal domain of lumazine protein, whereas the C-terminal domain lacks a ligand.
KW - Photobacterium leiognathi
KW - crystal structure
KW - lumazine protein
KW - luminescent bacteria
KW - riboflavin synthase
UR - http://www.scopus.com/inward/record.url?scp=49349084023&partnerID=8YFLogxK
U2 - 10.1016/j.jmb.2008.06.052
DO - 10.1016/j.jmb.2008.06.052
M3 - Article
C2 - 18602927
AN - SCOPUS:49349084023
SN - 0022-2836
VL - 382
SP - 44
EP - 55
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
IS - 1
ER -